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Conserved domains on  [gi|489519233|ref|WP_003424036|]
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ACT domain-containing protein [Clostridioides difficile]

Protein Classification

ACT domain-containing protein( domain architecture ID 11466474)

ACT domain-containing protein similar to vertebrate GATS-like proteins 2 and 3, which function as regulators of TORC1 signaling pathway through the GATOR complex

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACT-7 COG3603
ACT domain, ACT-7 family [Signal transduction mechanisms];
1-119 2.96e-66

ACT domain, ACT-7 family [Signal transduction mechanisms];


:

Pssm-ID: 442822 [Multi-domain]  Cd Length: 120  Bit Score: 195.81  E-value: 2.96e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519233   1 MKLKLLVEEYAVCRLNNDTKIPTWIDTERFYSITRTDDELSIVCLNNNIPSDVKSEKEWRILKILGPLDFSLVGILSKLS 80
Cdd:COG3603    2 LTLKLLPGEYAVCRLPPDAPIPAWALGSGFVSITRTPDELSIVCPEERVPAGVRAERGWRALKVEGPLDFSLTGILASLS 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489519233  81 SLLADNKISIFAISTYDTDYILVKEKDIENACKILNCNG 119
Cdd:COG3603   82 SPLAEAGISIFAVSTFDTDYLLVKEADLDRAVAALRAAG 120
 
Name Accession Description Interval E-value
ACT-7 COG3603
ACT domain, ACT-7 family [Signal transduction mechanisms];
1-119 2.96e-66

ACT domain, ACT-7 family [Signal transduction mechanisms];


Pssm-ID: 442822 [Multi-domain]  Cd Length: 120  Bit Score: 195.81  E-value: 2.96e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519233   1 MKLKLLVEEYAVCRLNNDTKIPTWIDTERFYSITRTDDELSIVCLNNNIPSDVKSEKEWRILKILGPLDFSLVGILSKLS 80
Cdd:COG3603    2 LTLKLLPGEYAVCRLPPDAPIPAWALGSGFVSITRTPDELSIVCPEERVPAGVRAERGWRALKVEGPLDFSLTGILASLS 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489519233  81 SLLADNKISIFAISTYDTDYILVKEKDIENACKILNCNG 119
Cdd:COG3603   82 SPLAEAGISIFAVSTFDTDYLLVKEADLDRAVAALRAAG 120
ACT_7 pfam13840
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ...
 55-116 4.12e-22

ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding.


Pssm-ID: 433519 [Multi-domain]  Cd Length: 65  Bit Score: 82.19  E-value: 4.12e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489519233   55 SEKEWRILKILGP-LDFSLVGILSKLSSLLADNKISIFAISTYDTDYILVKEKDIENACKILN 116
Cdd:pfam13840   2 SEDGWAKLSVVGAgLDFDVPGVVAKLTSPLAEAGISIFQISSYTTDYVLVPEEDLEKAVRALH 64
ACT_AK-like cd04868
ACT domains C-terminal to the catalytic domain of aspartokinase (AK; ...
 61-116 5.94e-04

ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase); This CD includes each of two ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). Typically, AK consists of two ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. Aspartokinase is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. One mechanism for the regulation of this pathway is by the production of several isoenzymes of aspartokinase with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli (EC), three different aspartokinase isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis (BS) isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as is a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium, and apparently, unique to cyanobacteria, are aspartokinases with two tandem pairs of ACT domains, C-terminal to the catalytic domain. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this AK family CD are the ACT domains of the Methylomicrobium alcaliphilum AK; the first enzyme of the ectoine biosynthetic pathway found in this bacterium and several other halophilic/halotolerant bacteria. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153140 [Multi-domain]  Cd Length: 60  Bit Score: 35.55  E-value: 5.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489519233  61 ILKILGPLDFSLVGILSKLSSLLADNKISIFAISTYDTDY---ILVKEKDIENACKILN 116
Cdd:cd04868    2 KVSIVGVGMRGTPGVAAKIFSALAEAGINVDMISQSESEVnisFTVDESDLEKAVKALH 60
 
Name Accession Description Interval E-value
ACT-7 COG3603
ACT domain, ACT-7 family [Signal transduction mechanisms];
1-119 2.96e-66

ACT domain, ACT-7 family [Signal transduction mechanisms];


Pssm-ID: 442822 [Multi-domain]  Cd Length: 120  Bit Score: 195.81  E-value: 2.96e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519233   1 MKLKLLVEEYAVCRLNNDTKIPTWIDTERFYSITRTDDELSIVCLNNNIPSDVKSEKEWRILKILGPLDFSLVGILSKLS 80
Cdd:COG3603    2 LTLKLLPGEYAVCRLPPDAPIPAWALGSGFVSITRTPDELSIVCPEERVPAGVRAERGWRALKVEGPLDFSLTGILASLS 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489519233  81 SLLADNKISIFAISTYDTDYILVKEKDIENACKILNCNG 119
Cdd:COG3603   82 SPLAEAGISIFAVSTFDTDYLLVKEADLDRAVAALRAAG 120
ACT_7 pfam13840
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ...
 55-116 4.12e-22

ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding.


Pssm-ID: 433519 [Multi-domain]  Cd Length: 65  Bit Score: 82.19  E-value: 4.12e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489519233   55 SEKEWRILKILGP-LDFSLVGILSKLSSLLADNKISIFAISTYDTDYILVKEKDIENACKILN 116
Cdd:pfam13840   2 SEDGWAKLSVVGAgLDFDVPGVVAKLTSPLAEAGISIFQISSYTTDYVLVPEEDLEKAVRALH 64
ACT_AK-like cd04868
ACT domains C-terminal to the catalytic domain of aspartokinase (AK; ...
 61-116 5.94e-04

ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase); This CD includes each of two ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). Typically, AK consists of two ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. Aspartokinase is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. One mechanism for the regulation of this pathway is by the production of several isoenzymes of aspartokinase with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli (EC), three different aspartokinase isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis (BS) isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as is a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium, and apparently, unique to cyanobacteria, are aspartokinases with two tandem pairs of ACT domains, C-terminal to the catalytic domain. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this AK family CD are the ACT domains of the Methylomicrobium alcaliphilum AK; the first enzyme of the ectoine biosynthetic pathway found in this bacterium and several other halophilic/halotolerant bacteria. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153140 [Multi-domain]  Cd Length: 60  Bit Score: 35.55  E-value: 5.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489519233  61 ILKILGPLDFSLVGILSKLSSLLADNKISIFAISTYDTDY---ILVKEKDIENACKILN 116
Cdd:cd04868    2 KVSIVGVGMRGTPGVAAKIFSALAEAGINVDMISQSESEVnisFTVDESDLEKAVKALH 60
ACT_AK-like_2 cd04892
ACT domains C-terminal to the catalytic domain of aspartokinase (AK; ...
 71-116 2.93e-03

ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase); This CD includes the second of two ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). The exception in this group, is the inclusion of the first ACT domain of the bifunctional aspartokinase - homoserine dehydrogenase-like enzyme group (ACT_AKi-HSDH-ThrA-like_1) which includes the monofunctional, threonine-sensitive, aspartokinase found in Methanococcus jannaschii and other related archaeal species. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. AK is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. One mechanism for the regulation of this pathway is by the production of several isoenzymes of AK with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli (EC), three different AK isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis (BS) isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as is a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium, and apparently, unique to cyanobacteria, are AKs with two tandem pairs of ACT domains, C-terminal to the catalytic domain. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this CD are the ACT domains of the Methylomicrobium alcaliphilum AK; the first enzyme of the ectoine biosynthetic pathway found in this bacterium and several other halophilic/halotolerant bacteria. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153164 [Multi-domain]  Cd Length: 65  Bit Score: 34.01  E-value: 2.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489519233  71 SLVGILSKLSSLLADNKISIFAISTYDTDY---ILVKEKDIENACKILN 116
Cdd:cd04892   12 GTPGVAARIFSALAEAGINIIMISQGSSEVnisFVVDEDDADKAVKALH 60
MetL1 COG0527
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ...
 71-115 4.13e-03

Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440293 [Multi-domain]  Cd Length: 407  Bit Score: 35.44  E-value: 4.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489519233  71 SLVGILSKLSSLLADNKISIFAISTYDTDY---ILVKEKDIENACKIL 115
Cdd:COG0527  351 SHPGVAARMFSALAEAGINIRMISQGSSEIsisVVVDEEDAEKAVRAL 398
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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